ID A0A0Q1AJ60_9CORY Unreviewed; 230 AA.
AC A0A0Q1AJ60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Heme oxygenase {ECO:0000313|EMBL:KQB86822.1};
DE EC=1.14.99.3 {ECO:0000313|EMBL:KQB86822.1};
GN Name=hmuO {ECO:0000313|EMBL:KQB86822.1};
GN ORFNames=Clow_01030 {ECO:0000313|EMBL:KQB86822.1};
OS Corynebacterium lowii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB86822.1, ECO:0000313|Proteomes:UP000050488};
RN [1] {ECO:0000313|EMBL:KQB86822.1, ECO:0000313|Proteomes:UP000050488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130206 {ECO:0000313|EMBL:KQB86822.1,
RC ECO:0000313|Proteomes:UP000050488};
RA Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT human clinical disease and and emended description of Corynebacterium
RT mastiditis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQB86822.1}.
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DR EMBL; LKEV01000002; KQB86822.1; -; Genomic_DNA.
DR RefSeq; WP_055177167.1; NZ_LKEV01000002.1.
DR AlphaFoldDB; A0A0Q1AJ60; -.
DR STRING; 1544413.Clow_01030; -.
DR PATRIC; fig|1544413.3.peg.1037; -.
DR OrthoDB; 5493802at2; -.
DR Proteomes; UP000050488; Unassembled WGS sequence.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR CDD; cd19165; HemeO; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR InterPro; IPR002051; Haem_Oase.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR PANTHER; PTHR10720; HEME OXYGENASE; 1.
DR PANTHER; PTHR10720:SF0; HEME OXYGENASE; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PIRSF; PIRSF000343; Haem_Oase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR000343-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000343-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000343-2};
KW Oxidoreductase {ECO:0000313|EMBL:KQB86822.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050488}.
FT BINDING 16
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 23
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-2"
FT BINDING 144
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 191
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 230 AA; 26073 MW; D3F56644B3631DB8 CRC64;
MTSAILPSSS LAADLKAFTA TAHERAEEST FMTDLLDGKL SAHDFLRLQE QAWFFYSALE
EAAHCVSHGE RAGLIVDEAL DRTAALESDI AYLHRQFYGE GAAEEGTRQW RANVTPIPAT
VEYVERLQRI RDERDEIRLI AHHYVRCLGD LSGGQVIATM MRRNYGIAPE ALQFYRFEGI
AKLKPYKDNY RKNLDAMRLN PAERQTLLEE ATEAFVLNMN VFAGLERGEK
//
